|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
34-303 |
1.11e-116 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 338.99 E-value: 1.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 34 KKRVFSGIQPTGILHLGNYLGAIESW------------------------------------------------------ 59
Cdd:PRK00927 1 KKRVLSGIQPTGKLHLGNYLGAIKNWvelqdeyecffciadlhaltvpqdpeelrentrelaadylacgidpekstifvq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 60 --VSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQ 137
Cdd:PRK00927 81 shVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 138 GFNKKYGEFFPVPESILTSMK-KVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT--SEVTYDPAGRAG 214
Cdd:PRK00927 161 RFNNLYGEVFPVPEPLIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSErlREIRYDLPNKPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 215 VSNIVAVHAAVTGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTV 292
Cdd:PRK00927 241 VSNLLTIYSALSGESIEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASKT 320
|
330
....*....|.
gi 1804891951 293 CQEVKKLVGFL 303
Cdd:PRK00927 321 LKEVREAMGLL 331
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
33-303 |
2.12e-110 |
|
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tryptophanyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439950 [Multi-domain] Cd Length: 330 Bit Score: 323.15 E-value: 2.12e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 33 SKKRVFSGIQPTGILHLGNYLGAIESW----------------------------------------------------- 59
Cdd:COG0180 2 SKKRVLSGIQPTGRLHLGNYLGALKNWvelqdeyecfffiadlhalttpqdpeelrentrevaadylaagldpekstifv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 60 ---VSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDL 135
Cdd:COG0180 82 qsdVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKENvNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 136 AQGFNKKYGEFFPVPESILT-SMKKVKSLrDPSAKMSKSDpdkLATVRITDSPEEIVQKFRKAVTDfTSEVTYDPAGRAG 214
Cdd:COG0180 162 ARRFNHRYGEVFPEPEALIPeEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTD-SERLRYDDPGKPE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 215 VSNIVAVHAAVTG-LSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYT 291
Cdd:COG0180 237 VCNLFTIYSAFSGkEEVEELEAeyRAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAIAAK 316
|
330
....*....|..
gi 1804891951 292 VCQEVKKLVGFL 303
Cdd:COG0180 317 TLAEVREAMGLL 328
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
36-255 |
3.20e-93 |
|
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding
Pssm-ID: 173903 [Multi-domain] Cd Length: 280 Bit Score: 277.54 E-value: 3.20e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 36 RVFSGIQPTGILHLGNYLGAIESW-------------------------------------------------------- 59
Cdd:cd00806 1 RVLSGIQPSGSLHLGHYLGAFRFWvwlqeagyelfffiadlhaltvkqldpeelrqntrenakdylacgldpekstiffq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 60 --VSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDgTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQ 137
Cdd:cd00806 81 sdVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESV-NIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 138 GFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSN 217
Cdd:cd00806 160 RFNKLYGEIFPKPAALLSKGAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1804891951 218 IVAVHAAVTGLSVEEVVR----RSAGMNTARYKLAVADAVIE 255
Cdd:cd00806 238 LVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQE 279
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
33-302 |
6.36e-67 |
|
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members of the family have a pfam00458 domain amino-terminal to the region described by this model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 272975 [Multi-domain] Cd Length: 327 Bit Score: 212.19 E-value: 6.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 33 SKKRVFSGIQPTGILHLGNYLGAIESW----------------------------------------------------- 59
Cdd:TIGR00233 1 KKFRVLTGIQPSGKMHLGHYLGAIQTKwlqqfgvelficiadlhaitvkqtdpdalrkareelaadylavgldpektfif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 60 ----VSEHTQLSWILSCMVRLPRLQHLHQWKAKTtkQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDL 135
Cdd:TIGR00233 81 lqsdYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 136 AQGFNKKYGEFFPVPESILT-SMKKVKSLRDpsAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAG 214
Cdd:TIGR00233 159 AERFNKKFKNFFPKPESLISkFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 215 VSNIVAVHAAVT-----GLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEklKLDKDHLEKVLQIGSAKAKE 287
Cdd:TIGR00233 235 VPNLLVIYQYLSfflidDDKLKEIYEayKSGKLGYGECKKALIEVLQEFLKEIQERRA--EIAEEILDKILEPGAKKARE 312
|
330
....*....|....*
gi 1804891951 288 LAYTVCQEVKKLVGF 302
Cdd:TIGR00233 313 TANKTLADVYKAMGL 327
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
30-258 |
8.38e-41 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 143.19 E-value: 8.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 30 QKDSKKRVFSGIQPTGILHLGnYLGAIESWVS------------------------------------------------ 61
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGPLHLG-YLVPLMKLRQfqqaghevffligdlhaiigdpsksperkllsretvlenaikaqlacg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 62 ---------------EHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG--TVGLLTYPVLQAADILLYKSTHVPVGED 124
Cdd:pfam00579 80 ldpekaeivnnsdwlEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGPgiSLGEFTYPLLQAYDILLLKADLQPGGSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 125 QVQHMELVQDLAQGFNKKygeFFPVPESILTsmkKVKSLRDPSAKMSKSDPdkLATVRITDSPEEIVQKFRKAVTDFTSE 204
Cdd:pfam00579 160 QWGNIELGRDLARRFNKK---IFKKPVGLTN---PLLTGLDGGKKMSKSAG--NSAIFLDDDPESVYKKIQKAYTDPDRE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1804891951 205 VTYDPAGRAGVSN-IVAVHAAVTGLSV---------EEVVRRSAGMNtarYKLAVADAVIEKFA 258
Cdd:pfam00579 232 VRKDLKLFTFLSNeEIEILEAELGKSPyreaeellaREVTGLVHGGD---LKKAAAEAVNKLLQ 292
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
34-303 |
1.11e-116 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 338.99 E-value: 1.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 34 KKRVFSGIQPTGILHLGNYLGAIESW------------------------------------------------------ 59
Cdd:PRK00927 1 KKRVLSGIQPTGKLHLGNYLGAIKNWvelqdeyecffciadlhaltvpqdpeelrentrelaadylacgidpekstifvq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 60 --VSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQ 137
Cdd:PRK00927 81 shVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 138 GFNKKYGEFFPVPESILTSMK-KVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT--SEVTYDPAGRAG 214
Cdd:PRK00927 161 RFNNLYGEVFPVPEPLIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSErlREIRYDLPNKPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 215 VSNIVAVHAAVTGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTV 292
Cdd:PRK00927 241 VSNLLTIYSALSGESIEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASKT 320
|
330
....*....|.
gi 1804891951 293 CQEVKKLVGFL 303
Cdd:PRK00927 321 LKEVREAMGLL 331
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
33-303 |
2.12e-110 |
|
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tryptophanyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439950 [Multi-domain] Cd Length: 330 Bit Score: 323.15 E-value: 2.12e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 33 SKKRVFSGIQPTGILHLGNYLGAIESW----------------------------------------------------- 59
Cdd:COG0180 2 SKKRVLSGIQPTGRLHLGNYLGALKNWvelqdeyecfffiadlhalttpqdpeelrentrevaadylaagldpekstifv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 60 ---VSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDL 135
Cdd:COG0180 82 qsdVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKENvNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 136 AQGFNKKYGEFFPVPESILT-SMKKVKSLrDPSAKMSKSDpdkLATVRITDSPEEIVQKFRKAVTDfTSEVTYDPAGRAG 214
Cdd:COG0180 162 ARRFNHRYGEVFPEPEALIPeEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTD-SERLRYDDPGKPE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 215 VSNIVAVHAAVTG-LSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYT 291
Cdd:COG0180 237 VCNLFTIYSAFSGkEEVEELEAeyRAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAIAAK 316
|
330
....*....|..
gi 1804891951 292 VCQEVKKLVGFL 303
Cdd:COG0180 317 TLAEVREAMGLL 328
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
36-255 |
3.20e-93 |
|
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding
Pssm-ID: 173903 [Multi-domain] Cd Length: 280 Bit Score: 277.54 E-value: 3.20e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 36 RVFSGIQPTGILHLGNYLGAIESW-------------------------------------------------------- 59
Cdd:cd00806 1 RVLSGIQPSGSLHLGHYLGAFRFWvwlqeagyelfffiadlhaltvkqldpeelrqntrenakdylacgldpekstiffq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 60 --VSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDgTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQ 137
Cdd:cd00806 81 sdVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESV-NIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 138 GFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSN 217
Cdd:cd00806 160 RFNKLYGEIFPKPAALLSKGAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1804891951 218 IVAVHAAVTGLSVEEVVR----RSAGMNTARYKLAVADAVIE 255
Cdd:cd00806 238 LVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQE 279
|
|
| PLN02886 |
PLN02886 |
aminoacyl-tRNA ligase |
23-303 |
1.30e-74 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215478 [Multi-domain] Cd Length: 389 Bit Score: 233.94 E-value: 1.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 23 SAAAPALQKDS------KKRVFSGIQPTGILHLGNYLGAIESW------------------------------------- 59
Cdd:PLN02886 29 ATAATAPEKEAppkvarKKRVVSGVQPTGSIHLGNYLGAIKNWvalqetydtffcvvdlhaitlphdprelgkatrstaa 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 60 -------------------VSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQ-KHDGTVGLLTYPVLQAADILLYKSTHV 119
Cdd:PLN02886 109 iylacgidpskasvfvqshVPAHAELMWLLSCSTPIGWLNKMIQFKEKSRKAgDENVGVGLLTYPVLMASDILLYQADLV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 120 PVGEDQVQHMELVQDLAQGFNKKYG------------EFFPVPES-ILTSMKKVKSLRDPSAKMSKSDPDKLATVRITDS 186
Cdd:PLN02886 189 PVGEDQKQHLELTRDIAERVNNLYGgrkwkklggrggSVFKVPEAlIPPAGARVMSLTDGTSKMSKSAPSDQSRINLLDP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 187 PEEIVQKFRKAVTDFTSEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVRRSAGMNTARYKLAVADAVIEKFAPIKREIEK 266
Cdd:PLN02886 269 PDVIANKIKRCKTDSFPGLEFDNPERPECNNLLSIYQLVTGKTKEEVLAECGDMRWGDFKPLLTDALIEHLSPIQVRYEE 348
|
330 340 350
....*....|....*....|....*....|....*..
gi 1804891951 267 LKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKLVGFL 303
Cdd:PLN02886 349 IMSDPSYLDSVLKEGADAAAEIADRTLANVYQAMGFV 385
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
33-302 |
6.36e-67 |
|
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members of the family have a pfam00458 domain amino-terminal to the region described by this model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 272975 [Multi-domain] Cd Length: 327 Bit Score: 212.19 E-value: 6.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 33 SKKRVFSGIQPTGILHLGNYLGAIESW----------------------------------------------------- 59
Cdd:TIGR00233 1 KKFRVLTGIQPSGKMHLGHYLGAIQTKwlqqfgvelficiadlhaitvkqtdpdalrkareelaadylavgldpektfif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 60 ----VSEHTQLSWILSCMVRLPRLQHLHQWKAKTtkQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDL 135
Cdd:TIGR00233 81 lqsdYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 136 AQGFNKKYGEFFPVPESILT-SMKKVKSLRDpsAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAG 214
Cdd:TIGR00233 159 AERFNKKFKNFFPKPESLISkFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 215 VSNIVAVHAAVT-----GLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEklKLDKDHLEKVLQIGSAKAKE 287
Cdd:TIGR00233 235 VPNLLVIYQYLSfflidDDKLKEIYEayKSGKLGYGECKKALIEVLQEFLKEIQERRA--EIAEEILDKILEPGAKKARE 312
|
330
....*....|....*
gi 1804891951 288 LAYTVCQEVKKLVGF 302
Cdd:TIGR00233 313 TANKTLADVYKAMGL 327
|
|
| PRK12282 |
PRK12282 |
tryptophanyl-tRNA synthetase II; Reviewed |
33-301 |
1.69e-45 |
|
tryptophanyl-tRNA synthetase II; Reviewed
Pssm-ID: 183400 [Multi-domain] Cd Length: 333 Bit Score: 156.55 E-value: 1.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 33 SKKRVFSGIQPTGILHLGNYLGA--------------------------------------------------------- 55
Cdd:PRK12282 1 TKPIILTGDRPTGKLHLGHYVGSlknrvalqneheqfvliadqqaltdnaknpekirrnilevaldylavgidpakstif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 56 IESWVSEHTQLSWILSCMVRLPRLQHLHQWKAKTtKQKHDG---TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELV 132
Cdd:PRK12282 81 IQSQIPELAELTMYYMNLVTVARLERNPTVKTEI-AQKGFGrsiPAGFLTYPVSQAADITAFKATLVPVGDDQLPMIEQT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 133 QDLAQGFNKKYG-EFFPVPESILTSMKKVKSLrDPSAKMSKSDPDKLAtvrITDSPEEIVQKFRKAVTDfTSEVTYDPAG 211
Cdd:PRK12282 160 REIVRRFNSLYGtDVLVEPEALLPEAGRLPGL-DGKAKMSKSLGNAIY---LSDDADTIKKKVMSMYTD-PNHIRVEDPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 212 RAGVSNIVAVHAAV--TGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKE 287
Cdd:PRK12282 235 KVEGNVVFTYLDAFdpDKAEVAELKAhyQRGGLGDVKCKRYLEEVLQELLAPIRERRAEFAKDPGYVLEILKAGSEKARE 314
|
330
....*....|....
gi 1804891951 288 LAYTVCQEVKKLVG 301
Cdd:PRK12282 315 VAAQTLSEVKDAMG 328
|
|
| PRK12556 |
PRK12556 |
tryptophanyl-tRNA synthetase; Provisional |
32-302 |
3.87e-41 |
|
tryptophanyl-tRNA synthetase; Provisional
Pssm-ID: 183592 [Multi-domain] Cd Length: 332 Bit Score: 145.25 E-value: 3.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 32 DSKKRVFSGIQPTGILHLGNYLGAIE-----------------------------------------SW----------- 59
Cdd:PRK12556 1 MSEKIMLTGIKPTGYPHLGNYIGAIKpalqmaknyegkalyfiadyhalnavhdpeqfrsytrevaaTWlslgldpedvi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 60 ------VSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-------TVGLLTYPVLQAADILLYKSTHVPVGEDQV 126
Cdd:PRK12556 81 fyrqsdVPEIFELAWILSCLTPKGLMNRAHAYKAKVDQNKEAGldldagvNMGLYTYPILMAADILLFQATHVPVGKDQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 127 QHMELVQDLAQGFNKKYGEFFPVPESILTSMKKVKSLRDpSAKMSKSDPDklaTVRITDSPEEIVQKFRKAVTDFT-SEV 205
Cdd:PRK12556 161 QHIEIARDIATYFNHTFGDTFTLPEYVIQEEGAILPGLD-GRKMSKSYGN---VIPLFAEQEKLRKLIFKIKTDSSlPNE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 206 TYDPAGragvSNIVAVHAA-VTGLSVEEV-VRRSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSA 283
Cdd:PRK12556 237 PKDPET----SALFTIYKEfATEEEVQSMrEKYETGIGWGDVKKELFRVVDRELAGPREKYAMYMNEPSLLDEALEKGAE 312
|
330
....*....|....*....
gi 1804891951 284 KAKELAYTVCQEVKKLVGF 302
Cdd:PRK12556 313 RAREIAKPNLAEIKKAIGF 331
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
30-258 |
8.38e-41 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 143.19 E-value: 8.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 30 QKDSKKRVFSGIQPTGILHLGnYLGAIESWVS------------------------------------------------ 61
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGPLHLG-YLVPLMKLRQfqqaghevffligdlhaiigdpsksperkllsretvlenaikaqlacg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 62 ---------------EHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG--TVGLLTYPVLQAADILLYKSTHVPVGED 124
Cdd:pfam00579 80 ldpekaeivnnsdwlEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGPgiSLGEFTYPLLQAYDILLLKADLQPGGSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 125 QVQHMELVQDLAQGFNKKygeFFPVPESILTsmkKVKSLRDPSAKMSKSDPdkLATVRITDSPEEIVQKFRKAVTDFTSE 204
Cdd:pfam00579 160 QWGNIELGRDLARRFNKK---IFKKPVGLTN---PLLTGLDGGKKMSKSAG--NSAIFLDDDPESVYKKIQKAYTDPDRE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1804891951 205 VTYDPAGRAGVSN-IVAVHAAVTGLSV---------EEVVRRSAGMNtarYKLAVADAVIEKFA 258
Cdd:pfam00579 232 VRKDLKLFTFLSNeEIEILEAELGKSPyreaeellaREVTGLVHGGD---LKKAAAEAVNKLLQ 292
|
|
| PRK12284 |
PRK12284 |
tryptophanyl-tRNA synthetase; Reviewed |
36-301 |
6.69e-30 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237036 [Multi-domain] Cd Length: 431 Bit Score: 117.41 E-value: 6.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 36 RVFSGIQPTGILHLGNYLGAIE-----------------------------------------SW--------------- 59
Cdd:PRK12284 4 RVLTGITTTGTPHLGNYAGAIRpaiaasrqpgvesfyfladyhalikcddpariqrstleiaaTWlaagldpervtfyrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 60 --VSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-------TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHME 130
Cdd:PRK12284 84 sdIPEIPELTWLLTCVAGKGLLNRAHAYKAAVDKNVAAGedpdagvTAGLFMYPVLMAADILMFNAHKVPVGRDQIQHIE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 131 LVQDLAQGFNKKYG-EFFPVPESILTsmKKVKSL-----RdpsaKMSKSDPDklaTVRITDSPEEIVQKFRKAVTDftSE 204
Cdd:PRK12284 164 MARDIAQRFNHLYGgEFFVLPEAVIE--ESVATLpgldgR----KMSKSYDN---TIPLFAPREELKKAIFSIVTD--SR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 205 VTYDPAGRAGvSNIVAVHAAVTGLSVEEVVRRS--AGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGS 282
Cdd:PRK12284 233 APGEPKDTEG-SALFQLYQAFATPEETAAFRQAlaDGIGWGDAKQRLFERIDRELAPMRERYEALIARPADIEDILLAGA 311
|
330
....*....|....*....
gi 1804891951 283 AKAKELAYTVCQEVKKLVG 301
Cdd:PRK12284 312 AKARRIATPFLAELREAVG 330
|
|
| PRK12283 |
PRK12283 |
tryptophanyl-tRNA synthetase; Reviewed |
33-301 |
5.67e-28 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 183401 [Multi-domain] Cd Length: 398 Bit Score: 111.58 E-value: 5.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 33 SKKRVFSGIQPTGILHLGNYLGA--------------------------------------------------------- 55
Cdd:PRK12283 1 FPDRVLSGMRPTGRLHLGHYHGVlknwvklqheyecfffvadwhaltthyetpevieknvwdmvidwlaagvdpaqatlf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 56 IESWVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHD--GTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQ 133
Cdd:PRK12283 81 IQSKVPEHAELHLLLSMITPLGWLERVPTYKDQQEKLKEKdlSTYGFLGYPLLQSADILIYRAGLVPVGEDQVPHVEMTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 134 DLAQGFNKKYG--------------------------------------------------------------------- 144
Cdd:PRK12283 161 EIARRFNHLYGrepgfeekaeaaikklgkkraklyhelrnayqeegddealeqarallqeqqnlsmgdrerlfgylegag 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 145 -EFFPVPESILTSMKKVKSLrdPSAKMSKSDPDklaTVRITDSPEEIVQKFRKAVTDFTSEVTYDPaGRAGVSNIVAVHA 223
Cdd:PRK12283 241 kIILPEPQALLTEASKMPGL--DGQKMSKSYGN---TIGLREDPESVTKKIRTMPTDPARVRRTDP-GDPEKCPVWQLHQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 224 AVTGLSVEEVVR---RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKLV 300
Cdd:PRK12283 315 VYSDEETKEWVQkgcRSAGIGCLECKQPVIDAILREQQPMRERAQKYEDDPSLVRAIVADGCEKARKVARETMRDVREAM 394
|
.
gi 1804891951 301 G 301
Cdd:PRK12283 395 G 395
|
|
| Tyr_Trp_RS_core |
cd00395 |
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ... |
63-255 |
7.08e-20 |
|
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS)/Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. These enzymes attach Tyr or Trp, respectively, to the appropriate tRNA. These class I enzymes are homodimers, which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173893 [Multi-domain] Cd Length: 273 Bit Score: 86.97 E-value: 7.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 63 HTQLSWILSCMVRLPRLQHLHQWKAKTtkqKHDGTVGLLTYPVLQAADILLYKSTH----VPVGEDQVQHMELVQDLAQG 138
Cdd:cd00395 100 HIQFLRDLGKHVYVNYMERKTSFQSRS---EEGISATEFTYPPLQAADFLLLNTTEgcdiQPGGSDQWGNITLGRELARR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 139 FNkkygeFFPVPESILTSMkkVKSLRDPsaKMSKSDPDKLATVRITDSPEEIVQKFRKAVtdftsevtydpagragVSNI 218
Cdd:cd00395 177 FN-----GFTIAEGLTIPL--VTKLDGP--KFGKSESGPKWLDTEKTSPYEFYQFWINAV----------------DSDV 231
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1804891951 219 VAVHAAVTGLSVEEVVRRSAGMNTAR----YKLAVADAVIE 255
Cdd:cd00395 232 INILKYFTFLSKEEIERLEQEQYEAPgyrvAQKTLAEEVTK 272
|
|
| PRK12285 |
PRK12285 |
tryptophanyl-tRNA synthetase; Reviewed |
97-199 |
6.43e-16 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237037 [Multi-domain] Cd Length: 368 Bit Score: 77.21 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 97 TVGLLTYPVLQAADILL------YKSTHVPVGEDQVQHMELVQDLAQGFNKKYGefFPVPESILtsMKKVKSLRdpSAKM 170
Cdd:PRK12285 179 NIGHIFYPATQAADILHpqleegPKPTLVPVGIDQDPHIRLTRDIAERLHGGYG--FIKPSSTY--HKFMPGLT--GGKM 252
|
90 100
....*....|....*....|....*....
gi 1804891951 171 SKSDPDklATVRITDSPEEIVQKFRKAVT 199
Cdd:PRK12285 253 SSSKPE--SAIYLTDDPETVKKKIMKALT 279
|
|
| PRK08560 |
PRK08560 |
tyrosyl-tRNA synthetase; Validated |
95-197 |
7.96e-09 |
|
tyrosyl-tRNA synthetase; Validated
Pssm-ID: 236286 [Multi-domain] Cd Length: 329 Bit Score: 55.64 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 95 DGTVGLLTYPVLQAADILlYKSTHVPV-GEDQVQ-HMeLVQDLAQGFNkkygefFPVPESILTSMkkVKSLRDPSAKMSK 172
Cdd:PRK08560 148 EPDVSKLVYPLMQVADIF-YLDVDIAVgGMDQRKiHM-LAREVLPKLG------YKKPVCIHTPL--LTGLDGGGIKMSK 217
|
90 100
....*....|....*....|....*
gi 1804891951 173 SDPDklATVRITDSPEEIVQKFRKA 197
Cdd:PRK08560 218 SKPG--SAIFVHDSPEEIRRKIKKA 240
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
37-174 |
2.91e-07 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 49.02 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 37 VFSGIQPTGILHLGNYLGAIESWV--SEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTV--------GLLTYPVL 106
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFlaQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVerwierikEDVEYMFL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1804891951 107 QAADILL---YKSTHVPVGEDQVQHMELVQDLAQGFNKKYgeffpVPESILTSMKKVKSLRdpsaKMSKSD 174
Cdd:cd00802 82 QAADFLLlyeTECDIHLGGSDQLGHIELGLELLKKAGGPA-----RPFGLTFGRVMGADGT----KMSKSK 143
|
|
| PTZ00126 |
PTZ00126 |
tyrosyl-tRNA synthetase; Provisional |
101-197 |
6.66e-06 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 240282 [Multi-domain] Cd Length: 383 Bit Score: 46.99 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 101 LTYPVLQAADILLYKSTHVPVGEDQVQhmelVQDLAqgfnKKYGEFFPVPES-ILTSMKKVKSLRDPSAKMSKSDPDklA 179
Cdd:PTZ00126 196 ILYPCMQCADIFYLKADICQLGMDQRK----VNMLA----REYCDKKKIKKKpIILSHHMLPGLLEGQEKMSKSDPN--S 265
|
90
....*....|....*...
gi 1804891951 180 TVRITDSPEEIVQKFRKA 197
Cdd:PTZ00126 266 AIFMEDSEEDVNRKIKKA 283
|
|
| PTZ00348 |
PTZ00348 |
tyrosyl-tRNA synthetase; Provisional |
91-210 |
9.72e-06 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 173541 [Multi-domain] Cd Length: 682 Bit Score: 46.82 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 91 KQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQGFNKKYgeffpvpESILTSMKKVKSLRDPSAKM 170
Cdd:PTZ00348 151 KTEGTLTAAQVLYPLMQCADIFFLKADICQLGLDQRKVNMLAREYCDLIGRKL-------KPVILSHHMLAGLKQGQAKM 223
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1804891951 171 SKSDPDklATVRITDSPEEIVQKFRKA----VTDFTSEVTYDPA 210
Cdd:PTZ00348 224 SKSDPD--SAIFMEDTEEDVARKIRQAycprVKQSASEITDDGA 265
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
101-197 |
1.44e-04 |
|
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) catalytic core domain. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formationof the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173902 [Multi-domain] Cd Length: 269 Bit Score: 42.59 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 101 LTYPVLQAADIL-LYKSTHVPvGEDQVQHMELVQDLAQGFNKK--YGEFFPvpesILTSMKkvkslrdpSAKMSKSDPDK 177
Cdd:cd00805 137 FIYPLLQAYDFVyLDVDLQLG-GSDQRGNITLGRDLIRKLGYKkvVGLTTP----LLTGLD--------GGKMSKSEGNA 203
|
90 100
....*....|....*....|
gi 1804891951 178 lATVRITDSPEEIVQKFRKA 197
Cdd:cd00805 204 -IWDPVLDSPYDVYQKIRNA 222
|
|
| PLN02486 |
PLN02486 |
aminoacyl-tRNA ligase |
98-196 |
1.54e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178104 Cd Length: 383 Bit Score: 39.73 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 98 VGLLTYPVLQAA-------DILLYKSTH----VPVGEDQVQHMELVQDLAQ--GFNKK---YGEFFPvpesiltsmkkvk 161
Cdd:PLN02486 191 IGKISFPAVQAApsfpssfPHLFGGKDKlrclIPCAIDQDPYFRMTRDVAPrlGYYKPaliESRFFP------------- 257
|
90 100 110
....*....|....*....|....*....|....*
gi 1804891951 162 SLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRK 196
Cdd:PLN02486 258 ALQGESGKMSASDPN--SAIYVTDTPKEIKNKINK 290
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
101-236 |
2.37e-03 |
|
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up tryptophanyl-tRNA synthetases at scores of 0 and below. The proteins found by this model have a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 272976 [Multi-domain] Cd Length: 378 Bit Score: 39.30 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891951 101 LTYPVLQAADIL-LYKSTHVPvGEDQVQHMELVQDLAQGFNKKYGEFFPVPesILTSMKKVKSLRDPSAKMSkSDPDKLA 179
Cdd:TIGR00234 164 FIYPLLQAYDFVyLNVDLQLG-GSDQWFNIRKGRDLARENLPSLQFGLTVP--LLTPADGEKMGKSLGGAVS-LDEGKYD 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1804891951 180 T-VRITDSPEEIVQKFRKAVTDFTSEVTYDpagragVSNIVAVHA-AVTGLSVEEVVRR 236
Cdd:TIGR00234 240 FyQKVINTPDELVKKYLKLFTFLGLEEIEQ------LVELKGPNPrEVKENLALEITKY 292
|
|
|